Crystal structure of a maltogenic amylase provides insights into a catalytic versatility (Q27619572)

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H J Kim

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T J Kim

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N C Ha

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S T Oh

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H S Cho

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M J Cho

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M J Kim

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H S Lee

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J W Kim

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K Y Choi

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K H Park

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B H Oh

Journal of Biological Chemistry

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language of work or name

English

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publication date

10 September 1999

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published in

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volume

274

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issue

37

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page(s)

26279-86

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cites work

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A neopullulanase-type alpha-amylase gene from Thermoactinomyces vulgaris R-47.

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Cloning and sequence analysis of the cyclomaltodextrinase gene from Bacillus sphaericus and expression in Escherichia coli cells

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Analysis of the gene encoding cyclomaltodextrinase from alkalophilic Bacillus sp. I-5 and characterization of enzymatic properties

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Genetics of a novel starch utilisation pathway present in Klebsiella oxytoca

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Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis

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Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose

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AMoRe: an automated package for molecular replacement

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The CCP4 suite: programs for protein crystallography

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Amino acid, peptide, and protein volume in solution

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Basic local alignment search tool

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Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution

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STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS

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Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity, and stability

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Crystal structure of recombinant soybean beta-amylase complexed with beta-cyclodextrin

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An extensively modified version of MolScript that includes greatly enhanced coloring capabilities

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Classical electrostatics in biology and chemistry

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Mechanisms of enzymatic glycoside hydrolysis

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Identifiers

DOI

10.1074/JBC.274.37.26279

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

10473583

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